Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance.
By M. Salverda, J. D. de Visser, Miriam Barlow. 2010
309 citations recorded by the source corpus.
Subfields: Biotechnology, Endocrinology, Molecular Medicine
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In Endocrinology
In Molecular Medicine
Citations in the corpus
- A Comprehensive, High-Resolution Map of a Gene’s Fitness Landscape (2014, methodology): “Fitness Landscape of TEM-1 b-Lactamase We chose to measure the DFE of the TEM-1 b-lactamase gene, a convenient model for the study of evolution and the fitness effects of mutations (Salverda et al. 2010; Soskine and Tawfik 2010).”
- Evolution-Based Functional Decomposition of Proteins (2015, unknown): “A), further examples of sector analysis for two other protein families - the dihydrofolate reductases (48) and the class A beta-lactamases (49) - are provided in Fig.”
- Capturing the mutational landscape of the beta-lactamase TEM-1 (2013, background): “Fourth, it is a model enzyme in biochemistry with well-defined 3D structure (20) and thermodynamical characteristics (21), and the impact of some stabilizing mutations in that enzyme has already been described (11, 14, 22– 24).”
- Evolvability as a function of purifying selection in TEM-1 β-lactamase. (2015, unknown): “Here, we focus on a powerful model system for protein evolution studies, TEM-1 b-lactamase (Bershtein et al., 2006; Salverda et al., 2010; Weinreich et al., 2006).”